Exploring the Structural and Functional role of α,β-unsaturated Ketoesters as Anti-Staphylococcal Agents Targeting Glutathione Peroxidase
Sushobhan MajiiD, Sayoni DamiD, Akanksha KumariiD, Himani Sharma, Naveen Sharma, Nirmal Kumar RanaiD, Asmita SamadderiD, Sudipta Bhattacharyya
Abstract
Multiple-drug resistant (MDR) Staphylococcus aureus strains (like methicillin-resistant S. aureus or MRSA) uses an arsenal of antioxidant enzymes to mitigate host-induced oxidative stress. Among them the non-canonical Staphylococcal glutathione peroxidase (SaGpx) plays a crucial role in bacterial redox homeostasis by reducing peroxides via thioredoxin-dependent pathways. Thus, enabling oxidative stress mitigation during host infection. Despite its importance in S. aureus, its role in bacterial pathogenesis remains unexplored. This study aimed to elucidate the possible role of SaGpx in Staphylococcal virulence. First, we determined the high-resolution crystal structure of SaGpx (at 1.65 [A] resolution) using X-ray crystallography. Guided by the catalytic cleft architecture of SaGpx, small-molecule based inhibitors were then rationally designed and synthesized. These inhibitors exhibited good binding affinity to SaGpx and complete enzymatic blockade. These inhibitors exhibited potent anti-S. aureus activity (MICs 6.25-31.25 M) along with no cytotoxicity in L929 fibroblast wound-healing assays. Furthermore, the in vivo antibacterial ability of these inhibitors was evaluated using S. aureus-infected skin wound mouse model, where these compounds show potent antibacterial and wound healing ability supported by subsequent histological as well as immunohistochemical analysis. These findings suggest SaGpx as a possible virulence determinant in S. aureus and position these synthesized inhibitors as promising antivirulence therapeutics. HighlightsO_LIThe high-resolution crystal structure of Staphylococcal glutathione peroxidase is solved. C_LIO_LIBased on the SaGpx catalytic site, ,{beta}-unsaturated ketoesters derivatives are synthesized. C_LIO_LISynthesized ,{beta}-unsaturated ketoesters derivatives inhibit SaGpx activity and binds the protein at M range. C_LIO_LISynthesized ,{beta}-unsaturated ketoesters derivatives show in vitro antibacterial activity against S. aureus at low M range. C_LIO_LISynthesized ,{beta}-unsaturated ketoesters derivatives show in vivo antibacterial and wound healing ability S. aureus-infected skin wound mouse model. C_LI
02 /Specification & Classification
Click any tag to browse matching papers- Citations
- 0
- Organism
- Assay
- Research Focus
- Approach
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Deciphering the Structure and Mechanism of SaGpx: A Non Canonical Glutathione Peroxidase from Staphylococcus aureus
Sushobhan Maji, Manjari Shukla, Sudipta Bhattacharyya·bioRxiv·Nov 24, 2025
- Development of non-β-Lactam covalent allosteric inhibitors targeting PBP2a in Methicillin-Resistant Staphylococcus aureus
Bogdan M. Benin, Rupak Kharel, … Woo Shik Shin·bioRxiv·May 29, 2024
- Isopropoxy benzene guanidine kills Staphylococcus aureus without detectable resistance
- The β-lactam adjuvant guanosine potentiates anti-folate antibiotics and pyrimidine synthesis inhibitors by depleting thymidine in methicillin-resistant Staphylococcus aureus
Aaron Christopher Nolan, Jessica Blaise Kelly, … James P. O’Gara·Antimicrobial Agents and ChemotherapyPeer-reviewed·Jun 10, 2026
- Metabolic reprogramming and flux to cell envelope precursors in a pentose phosphate pathway mutant increases MRSA resistance to β-lactam antibiotics
M. S. Zeden, L. A. Gallagher, … J. P. O'Gara·bioRxiv·Mar 3, 2023
- GpoA Glutathione Peroxidase Links Oxidative Stress Response, Antibiotic Persistence, and Virulence in Streptococcus pneumoniae
Victoria E. Zappia, Mirelys Hernandez-Morfa, … José Echenique·Free Radical Biology and MedicinePeer-reviewed·Apr 21, 2026